Abstract
Background Despite development in Anti Retroviral Therapy (ART), reports of HIV infection remains in continuous momentum and a cure seems to be imaginary. Raltegravir, an Integrase (IN) inhibitor, provides some life expectancy to patients on salvage therapy. Nowadays, IN inhibitors reported with resistance and shows cross resistance to other drugs in this class. Human Lens Epithelium Derived Growth Factor (LEDGF)/p75 plays a vital role in the HIV life cycle and its importance has been shown in numerous studies. In the LEDGF/p75 IN complex, LEDGF binds to IN at a region other than the catalytic active site. Thus, we tried computationally to approach these IN-LEDGF interaction sites as a novel target in therapy.
Highlights
Despite development in Anti Retroviral Therapy (ART), reports of HIV infection remains in continuous momentum and a cure seems to be imaginary
Human Lens Epithelium Derived Growth Factor (LEDGF)/p75 plays a vital role in the HIV life cycle and its importance has been shown in numerous studies
ResultsIt is known that Ile[365] establishes a hydrogen bond with backbone carbonyl group of IN Gln[168] whereas Asp[366] of Lens Epithelium Derived Growth Factor (LEDGF)/p75 forms a hydrogen bond with Glu[170], on similar basis it was found that AMP_1071 exhibits hydrogen bonding with Gln[95] of one monomer and Gln[168], Hie[171], and Thr[174] of another monomer of IN
Summary
Despite development in Anti Retroviral Therapy (ART), reports of HIV infection remains in continuous momentum and a cure seems to be imaginary. Raltegravir, an Integrase (IN) inhibitor, provides some life expectancy to patients on salvage therapy. IN inhibitors reported with resistance and shows cross resistance to other drugs in this class. Human Lens Epithelium Derived Growth Factor (LEDGF)/p75 plays a vital role in the HIV life cycle and its importance has been shown in numerous studies. In the LEDGF/p75 IN complex, LEDGF binds to IN at a region other than the catalytic active site. We tried computationally to approach these IN-LEDGF interaction sites as a novel target in therapy
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